Research workbench
The crystal structure of the staphylococcus aureus fatty acid kinase (fak) B1 protein loaded with palmitic acid to 1.83 ångström resolution
Analyse The crystal structure of the staphylococcus aureus fatty acid kinase (fak) B1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UTO
- Type
- protein
- Length
- 575 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- X5EH37
- Ligands
- PLM
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 288 | — | X5EH37 |
| B | — | protein | 287 | — | X5EH37 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UTO · The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt X5EH37
- Elsewhere: RCSB PDB 5UTO · PDBe 5UTO · UniProt X5EH37
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